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Article

Enhancement in catalytic activity of CotA-laccase from Bacillus pumilus W3 via site-directed mutagenesis.

Journal of bioscience and bioengineering - 1 Apr 2020

Xu Kai-Zhong, Wang Hao-Ran, Wang Ya-Jing, Xia Jing, Ma Hui, Cai Yu-Jie, Liao Xiang-Ru, Guan Zheng-Bing

Abstract excerpt

CotA-laccases are potential enzymes that are widely used in decolorization of dyes and degradation of toxic substances. In this study, a novel CotA-laccase gene from Bacillus pumilus W3 was applied for rational design. After a series of site-directed genetic mutations, the mutant S208G/F227A showed a 5.1-fold higher catalytic efficiency (kcat/Km) than the wild-type CotA-laccase did. The optimal pH of S208G/F227A...

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Identifiers

PMID: 31672431
DOI: 10.1016/j.jbiosc.2019.09.020

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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